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Mosaic evolution of prepropancreatic polypeptide.

H Yamamoto, K Nata, H Okamoto

    The Journal of Biological Chemistry
    |May 15, 1986
    PubMed
    Summary
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    Researchers identified rat pancreatic polypeptide precursor cDNA, revealing high homology to human sequences but a divergent C-terminal peptide, suggesting unique evolutionary patterns in prohormone development.

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Evolutionary Biology

    Background:

    • Pancreatic polypeptide (PP) is a peptide hormone regulating gastrointestinal and pancreatic functions.
    • PP is synthesized in pancreatic islets of Langerhans.
    • Understanding PP precursor structure is key to its physiological roles.

    Purpose of the Study:

    • To isolate and characterize cDNA clones encoding the rat pancreatic polypeptide precursor.
    • To compare the rat PP precursor sequence with its human counterpart.
    • To investigate evolutionary conservation and divergence in prohormone processing.

    Main Methods:

    • Isolation of cDNA clones from a rat islet cDNA library.
    • Determination of nucleic acid sequences of the isolated clones.

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  • Comparative sequence analysis of rat and human PP precursors.

    • Main Results:

    • Successfully isolated and sequenced rat pancreatic polypeptide precursor cDNA.
    • Rat PP precursor shares high sequence homology with human PP precursor, including the signal peptide and PP sequence.
    • The C-terminal peptide of the rat precursor shows significant divergence from the human precursor and lacks similarity to known mammalian PP precursor products.

    Conclusions:

    • The rat pancreatic polypeptide precursor structure is conserved in its N-terminal regions but divergent in its C-terminal peptide.
    • This mosaic pattern of conservation and divergence offers a unique perspective on prohormone evolution.
    • Further studies are needed to elucidate the functional significance of the divergent C-terminal peptide in rats.